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Characterization of Components of Z-bands in the Fibrillar Flight Muscle of Drosophila melanogaster

By Judith D. Saide, Stephen Chin-bow, Judith Hogan-sheldon, Lizette Busquets-turner, Jim O. Vigoreaux, Katrin Valgeirsdottir and Mary Lou Pardue


Abstract. Twelve monoclonal antibodies have been raised against proteins in preparations of Z-disks iso-lated from Drosophila melanogaster flight muscle. The monoclonal antibodies that recognized Z-hand compo-nents were identified by immunofluorescence micros-copy of flight muscle myofibrils. These antibodies have identified three Z-disk antigens on immunoblots of myofibrillar proteins. Monoclonal antibodies c~:1-4 recognize a 90-100-kD protein which we identify as o~-actinin on the basis of cross-reactivity with antibod-ies raised against honeybee and vertebrate ot-actinins. Monoclonal antibodies P:l-4 bind to the high molecu-lar mass protein, projectin, a component of connecting filaments that link the ends of thick filaments to the Z-band in insect asynchronous flight muscles. The anti-projectin antibodies also stain synchronous mus-cle, but, surprisingly, the epitopes here are within the T HE Z-band is an electron-dense structural component of striated muscle. It serves as an attachment site for thin filaments and transmits tension between neighbor-ing sarcomeres during contraction. Electron micrographs of both vertebrate muscle and insect fibrillar muscle show Z-bands with a highly ordered, almost crystalline, appear-ance in cross section (for reviews see 1, 4, 12, 40, 42). Sev-eral Z-band proteins have been identified from both ver

Year: 2008
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